10ay

Cryo-EM structure of CRBN-DDB1 in complex with HBS1L and TNG961

Method: ELECTRON MICROSCOPY Dmax: 191.9 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

HBS1-like protein

Homo sapiens

UniProt Q9Y450

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 478–684 Chain D; UniProt 478–684 Fragment:domain 2 + domain 3 Protein cereblon × 2 (Q96SW2) DNA damage-binding protein 1 × 2 (Q16531) A1C4S N-{6-[(3R)-2,6-dioxopiperidin-3-yl]naphthalen-1-yl}-N'-{2-[6-(trifluoromethyl)-1-benzothiophen-2-yl]propan-2-yl}urea × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;0.1 M HEPES (pH 7.5), 0.24 M sodium chloride, 3 mM TCEP, 0.2 % n-octylglucoside cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HBS1L_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–208; UniProt 478–684 Author chain D; PDBConstruct 2–208; UniProt 478–684

Protein cereblon

Homo sapiens

UniProt Q96SW2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 40–442 Chain E; UniProt 40–442 Not recorded HBS1-like protein × 2 (Q9Y450) DNA damage-binding protein 1 × 2 (Q16531) A1C4S N-{6-[(3R)-2,6-dioxopiperidin-3-yl]naphthalen-1-yl}-N'-{2-[6-(trifluoromethyl)-1-benzothiophen-2-yl]propan-2-yl}urea × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;0.1 M HEPES (pH 7.5), 0.24 M sodium chloride, 3 mM TCEP, 0.2 % n-octylglucoside cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

93 other PDB entries and 141 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CRBN_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–404; UniProt 40–442 Author chain E; PDBConstruct 2–404; UniProt 40–442

DNA damage-binding protein 1

Homo sapiens

UniProt Q16531

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 1–1140 Chain F; UniProt 1–1140 Not recorded HBS1-like protein × 2 (Q9Y450) Protein cereblon × 2 (Q96SW2) A1C4S N-{6-[(3R)-2,6-dioxopiperidin-3-yl]naphthalen-1-yl}-N'-{2-[6-(trifluoromethyl)-1-benzothiophen-2-yl]propan-2-yl}urea × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;0.1 M HEPES (pH 7.5), 0.24 M sodium chloride, 3 mM TCEP, 0.2 % n-octylglucoside cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

202 other PDB entries and 290 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DDB1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–1140; UniProt 1–1140 Author chain F; PDBConstruct 1–1140; UniProt 1–1140

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 10ay

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10ay
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10ay
Deposition date deposition_date2026-01-09
Structure title titleCryo-EM structure of CRBN-DDB1 in complex with HBS1L and TNG961
Keywords keywordsFOCAD, ribosome, PELO, ubiquitin, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier60.82
Radius of gyration Rg (electron density) rg_electron61.80
Forward intensity I(0) i01111920000.00
Molecular weight molecular_weight286610.0 kDa
Excluded volume excluded_volume361790 ų
Envelope volume envelope_volume517700 ų
Hydration-shell volume shell_volume75220 ų
Envelope diameter envelope_diameter209.4
Shell Rg shell_rg54.30
Envelope Rg envelope_rg60.93
Shape Rg shape_rg61.82
Total Rg total_rg61.51
Total atoms total_atoms40391
Residues n_residues2524
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax191.9
Rg (real space) rg_real61.72
Rg uncertainty (real space) rg_real_error2.11
I(0) (real space) i0_real1.1120e+09
I(0) uncertainty (real space) i0_real_error2.4200e+07
Rg (reciprocal space) rg_reciprocal59.98
I(0) (reciprocal space) i0_reciprocal1109000000.0000
Solution quality estimate total_estimate0.7532
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.3
Skewness Skewness skewness0.512
Kurtosis Kurtosis kurtosis-0.704
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha103200000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.665; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.793; Smooth: 0.001

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)